title: Characterization of thermostable cyclodextrinase from Clostridium thermohydrosulfuricum 39E.
abstract: Clostridium thermohydrosulfuricum 39E produced a cell-bound cyclodextrin (CD)-degrading enzyme (cyclodextrinase). It was partially purified 205-fold (specific activity, 14.5 U/mg of protein) by solubilizing with Triton X-100, ammonium sulfate treatment, and DEAE-Sepharose CL-6B column chromatography. The enzyme activity was found to be stable at pH 5.5 and 60 degrees C and optimally active at pH 6.0 and 65 degrees C. The enzyme preparation hydrolyzed CDs, with alpha-CD greater than beta-CD greater than gamma-CD, and displayed a putative multiple attack pattern. The enzyme activity was inhibited by p-chloromercuribenzoate but not by N-bromosuccinimide.
authors.affiliation: Michigan Biotechnology Institute, Lansing 48909.
authors.forename: B C
authors.initials: BC
authors.lastname: Saha
authors.forename: J G
authors.initials: JG
authors.lastname: Zeikus
mesh_terms: D003013:Clostridium / Q000201:enzymology*; D006026:Glycoside Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D006026:Glycoside Hydrolases; C048745:cyclomaltodextrinase